Worm Breeder's Gazette 12(2): 36 (January 1, 1992)
These abstracts should not be cited in bibliographies. Material contained herein should be treated as personal communication and should be cited as such only with the consent of the author.
The DEAD-box family of proteins includes RNA-dependent ATPases involved in processing both structural and messenger RNAs (Linder et al., Nature 337 (1989) 121-122). A number of DEAD-box proteins have been identified as translational initiation factors, including the mouse eIF-4 A1protein (Nielsen et al., NAR 13 (1985) 6867-6880)) and the recently-characterized ME31 Bprotein of Drosophila (de Valoir et al., Proc. Natl. Acad. Sci. USA 88 (1991) 2113-2117). The predicted translation product of EST D18 R(McCombie et al., this issue) is very similar to the C-terminal ends of these proteins, as well as other members of the DEAD-box family, suggesting that D18 Rtags an initiation-factor gene. EST D33 Falso matches these proteins.
The DEAH-box family includes putative RNA helicases involved in spliceosome assembly, and hence presumably in splice-site selection (Burgess et al., Cell 60 (1990) 705-717). The maleless gene of Drosophila, which regulates dosage compensation in males by binding multiple sites on the X chromosome, is also a DEAH-box protein (Kuroda et al., Cell 66 (1991) 935-947). Two ESTs with high similarity to yeast PRP16 (Burgess et al.), maleless, and other members of the DEAH-box family have been sequenced. EST H51 Rtags the DEAH-box region of the protein, the putative RNA helicase domain, which is highly conserved between members of the family. EST H57 Rtags a region similar to the C-terminal ends of PRP2 (Chen, J. and Lin. R. Nucl. Acids Res. 18 (1990) 6447) and PRP16 ;the maleless protein is significantly less similar to the PRP proteins in this region than is the C. elegans protein. We do not yet know whether H51 Rand H57 Rtag the same gene.
[See Figure 1]